Homologous Superfamily

Tryptophan RNA-binding attenuator protein-like domain superfamily (IPR016031)

Short name: Trp_RNA-bd_attenuator-like_dom

Overlapping entries


The tryptophan RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in Bacillus sp. by binding to the leader region of the nascent trp operon mRNA [PMID: 11914485]. The crystal structure of the Trp RNA-binding attenuation protein of Bacillus subtilis (mtrB, P19466) has been solved [PMID: 7715723]. TRAP forms an oligomeric ring consisting of 11 single-domain subunits, where each subunit adopts a double-stranded beta-helix structure with the appearance of a beta-sandwich of distinct architecture and jelly-roll fold. The 11 subunits are stabilised by 11 inter-subunit strands, forming a beta-wheel with a large central hole. TRAP is activated by binding to tryptophan in clefts between adjacent beta-strands, which induces conformational changes in the protein. Activated TRAP binds an mRNA target sequence consisting of 11 (G/U)AG repeats, separated by 2-3 spacer nucleotides. The spacer nucleotides do not make direct contact with the TRAP protein, but they do influence the conformation of the RNA, which might influence the specificity of TRAP [PMID: 15050822].

This superfamily represents a domain with a TRAP-like double-stranded beta-helix topology. This domain is found in TRAP proteins, as well as in the hypothetical protein SPyM3_0169 from Streptococcus pyogenes. SPyM3_0169 contains 9 domains per ring-like trimer, where each subunit contains three structural repeats.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.